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BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins

Journal of biomolecular NMR, 2013-04, Vol.55 (4), p.311-321

2013

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Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

Autophagy, 2009-07, Vol.5 (5), p.690-698

2009

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The Atg8 Family of Proteins-Modulating Shape and Functionality of Autophagic Membranes

Frontiers in genetics, 2017-08, Vol.8, p.109-109

2017

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Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-β Variants and Structural Analysis by Solution NMR Spectroscopy

PloS one, 2015-10, Vol.10 (10), p.e0139710

2015

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Transient Structure and SH3 Interaction Sites in an Intrinsically Disordered Fragment of the Hepatitis C Virus Protein NS5A

Journal of molecular biology, 2012-07, Vol.420 (4-5), p.310-323

2012

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Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation

Computational and structural biotechnology journal, 2024-12, Vol.23, p.417-430

2024

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Structural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous Trifluoroethanol

PloS one, 2015-11, Vol.10 (11), p.e0143647-e0143647

2015

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Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization

Scientific reports, 2017-07, Vol.7 (1), p.5979-12, Article 5979

2017

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The mammalian autophagy initiator complex contains 2 HORMA domain proteins

Autophagy, 2015-12, Vol.11 (12), p.2300-2308

2015

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Conformational Polymorphism in Autophagy-Related Protein GATE-16

Biochemistry (Easton), 2015-09, Vol.54 (35), p.5469-5479

2015

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Ras Homolog Enriched in Brain (Rheb) Enhances Apoptotic Signaling

The Journal of biological chemistry, 2010-10, Vol.285 (44), p.33979-33991

2010

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Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes

Viruses, 2015-07, Vol.7 (7), p.4119-4130

2015

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Preparation of a Functional GABARAP-Lipid Conjugate in Nanodiscs and its Investigation by Solution NMR Spectroscopy

Chembiochem : a European journal of chemical biology, 2010-09, Vol.11 (14), p.1967-1970

2010

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Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation

Cells (Basel, Switzerland), 2020-05, Vol.9 (5), p.1296

2020

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Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain

Biochemical and biophysical research communications, 2010-05, Vol.395 (3), p.426-431

2010

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Pyroglutamate-Modified Amyloid-β(3–42) Shows α-Helical Intermediates before Amyloid Formation

Biophysical journal, 2017-04, Vol.112 (8), p.1621-1633

2017

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Pyroglutamate-Modified Amyloid-[Beta](3-42) Shows α-Helical Intermediates before Amyloid Formation

Biophysical journal, 2017-04, Vol.112 (8), p.P1621

2017

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Structural Studies of Autophagy-Related Proteins

Methods in molecular biology (Clifton, N.J.), 2019, Vol.1880, p.17

2019

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Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies

Chemical science (Cambridge), 2016-01, Vol.7 (7), p.4492-4502

2016

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P4‐308: Pyroglutamate‐Modified Amyloid‐β(3‐42) Forms Transient a‐Helices Prior to Amyloid Formation

Alzheimer's & dementia, 2016-07, Vol.12 (7S_Part_24), p.P1151-P1152

2016

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PEASS(3-42) INCREASES AGGREGATION PROPENSITY OF ASS(1-42) BY ACCELERATING PRIMARY AND SECONDARY PATHWAYS

Alzheimer's & dementia, 2016-07, Vol.12 (7), p.P1152-P1152

2016

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PYROGLUTAMATE-MODIFIED AMYLOID-β(3-42) FORMS TRANSIENT A-HELICES PRIOR TO AMYLOID FORMATION

Alzheimer's & dementia, 2016-07, Vol.12 (7), p.P1151-P1152

2016

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P4‐309: Peass(3‐42) Increases Aggregation Propensity of ass(1‐42) by Accelerating Primary and Secondary Pathways

Alzheimer's & dementia, 2016-07, Vol.12 (7S_Part_24), p.P1152-P1152

2016

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The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation

Biophysical journal, 2015-10, Vol.109 (7), p.1483-1496

2015

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Structure and potential function of γ-aminobutyrate type A receptor-associated protein

The FEBS journal, 2009-09, Vol.276 (18), p.4989-5005

2009

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BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins

Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

The Atg8 Family of Proteins-Modulating Shape and Functionality of Autophagic Membranes

Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-β Variants and Structural Analysis by Solution NMR Spectroscopy

Transient Structure and SH3 Interaction Sites in an Intrinsically Disordered Fragment of the Hepatitis C Virus Protein NS5A

Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation

Structural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous Trifluoroethanol

Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization

The mammalian autophagy initiator complex contains 2 HORMA domain proteins

Conformational Polymorphism in Autophagy-Related Protein GATE-16

Ras Homolog Enriched in Brain (Rheb) Enhances Apoptotic Signaling

Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes

Preparation of a Functional GABARAP-Lipid Conjugate in Nanodiscs and its Investigation by Solution NMR Spectroscopy

Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation

Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain

Pyroglutamate-Modified Amyloid-β(3–42) Shows α-Helical Intermediates before Amyloid Formation

Pyroglutamate-Modified Amyloid-[Beta](3-42) Shows α-Helical Intermediates before Amyloid Formation

Structural Studies of Autophagy-Related Proteins

Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies

P4‐308: Pyroglutamate‐Modified Amyloid‐β(3‐42) Forms Transient a‐Helices Prior to Amyloid Formation

PEASS(3-42) INCREASES AGGREGATION PROPENSITY OF ASS(1-42) BY ACCELERATING PRIMARY AND SECONDARY PATHWAYS

PYROGLUTAMATE-MODIFIED AMYLOID-β(3-42) FORMS TRANSIENT A-HELICES PRIOR TO AMYLOID FORMATION

P4‐309: Peass(3‐42) Increases Aggregation Propensity of ass(1‐42) by Accelerating Primary and Secondary Pathways

The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation

Structure and potential function of γ-aminobutyrate type A receptor-associated protein

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